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(Synonyms: 2-氨基-3-甲基丁酸;Α-氨基异戊酸;ALPHA-氨基异戊酸;L-Aminovaleic Acid;1-2-Amino-3-Methylbutyric Acid) 目录号 : GC20105

Valine Chemical Structure

Cas No.:7004-03-7

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5g
¥200.00
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25g
¥600.00
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Sample solution is provided at 25 µL, 10mM.

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Chemical Properties

Cas No. 7004-03-7 SDF
别名 2-氨基-3-甲基丁酸;Α-氨基异戊酸;ALPHA-氨基异戊酸;L-Aminovaleic Acid;1-2-Amino-3-Methylbutyric Acid
分子式 C5H11NO2 分子量 117.08
溶解度 储存条件 Store at RT
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1 mM 8.5412 mL 42.7058 mL 85.4117 mL
5 mM 1.7082 mL 8.5412 mL 17.0823 mL
10 mM 0.8541 mL 4.2706 mL 8.5412 mL
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Research Update

Dietary Valine Ameliorated Gut Health and Accelerated the Development of Nonalcoholic Fatty Liver Disease of Laying Hens

Oxid Med Cell Longev 2021 Aug 23;2021:4704771.PMID:34484560DOI:10.1155/2021/4704771.

Valine is an important essential amino acid of laying hens. Dietary supplemented with BCAAs ameliorated gut microbiota, whereas elevated blood levels of BCAAs are positively associated with obesity, insulin resistance, and diabetes in both humans and rodents. General controlled nonrepressed (GCN2) kinase plays a crucial role in regulating intestinal inflammation and hepatic fatty acid homeostasis during amino acids deficiency, while GCN2 deficient results in enhanced intestinal inflammation and developed hepatic steatosis. However, how long-term dietary Valine impacts gut health and the development of nonalcoholic fatty liver disease (NAFLD) remains unknown. Hence, in the present study, we elucidated the effects of dietary Valine on intestinal barrier function, microbial homeostasis, and the development of NAFLD. A total of 960 healthy 33-weeks-old laying hens were randomly divided into five experimental groups and fed with Valine at the following different levels in a feeding trial that lasted 8 weeks: 0.59, 0.64, 0.69, 0.74, and 0.79%, respectively. After 8 weeks of treatment, related tissues and cecal contents were obtained for further analysis. The results showed that diet supplemented with Valine ameliorated gut health by improving intestinal villus morphology, enhancing intestinal barrier, decreasing cecum pathogenic bacteria abundances such as Fusobacteriota and Deferribacterota, and inhibiting inflammatory response mediated by GCN2. However, long-term intake of high levels of dietary Valine (0.74 and 0.79%) accelerated the development of NAFLD of laying hens by promoting lipogenesis and inhibiting fatty acid oxidation mediated by GCN2-eIF2α-ATF4. Furthermore, NAFLD induced by high levels of dietary Valine (0.74 and 0.79%) resulted in strengthening oxidative stress, ER stress, and inflammatory response. Our results revealed that high levels of Valine are a key regulator of gut health and the adverse metabolic response to NAFLD and suggested reducing dietary Valine as a new approach to preventing NAFLD of laying hens.

Evaluation of the Valine requirement of small-framed first cycle laying hens

Poult Sci 2019 Mar 1;98(3):1272-1279.PMID:30329096DOI:10.3382/ps/pey448.

An experiment was conducted to evaluate the total Valine (Val) requirement of first cycle laying hens from 41 to 60 wk of age. A total of 270 Hy-line W-36 laying hens were randomly assigned to 6 treatments with 15 replicate groups of 3 birds for each experimental unit. A Val deficient basal diet was formulated with corn and peanut meal with analyzed Val, Lys and crude protein concentrations of 0.515, 0.875, and 13.38%, respectively. Synthetic L-Val was supplemented to the basal diet in 0.070% increments to generate experimental diets containing 0.515, 0.585, 0.655, 0.725, 0.795, and 0.865% Val respectively. A controlled feeding program was applied during the experiment resulting in approximately 95 g feed intake per hen per day. Linear broken line, quadratic broken line, quadratic polynomial and exponential models were used to estimate the Val requirement of the hens based on hen-housed egg production (HHEP), egg mass (EM), and feed conversion ratio (FCR). Hen-housed egg production ranged from 48.3 to 81.4%, dependent upon dietary concentration of Val. Val requirements estimated by linear broken line, quadratic broken line, quadratic polynomial and exponential models were reported. Using the linear broken line model, the Val requirement was highest for egg mass, 597.3 mg/d, followed by egg production, 591.9 mg/d and lowest for FCR, 500.5 mg/d.

Valine Treatment Enhances Antimicrobial Component Production in Mammary Epithelial Cells and the Milk of Lactating Goats Without Influencing the Tight Junction Barrier

J Mammary Gland Biol Neoplasia 2023 Feb 18;28(1):3.PMID:36801983DOI:10.1007/s10911-023-09529-x.

The production of antimicrobial components and the formation of less-permeable tight junctions (TJs) are important in the defense system of lactating mammary glands and for safe dairy production. Valine is a branched-chain amino acid that is actively consumed in the mammary glands and promotes the production of major milk components like β-casein; additionally, branched-chain amino acids stimulate antimicrobial component production in the intestines. Therefore, we hypothesized that Valine strengthens the mammary gland defense system without influencing milk production. We investigated the effects of Valine in vitro using cultured mammary epithelial cells (MECs) and in vivo using the mammary glands of lactating Tokara goats. Valine treatment at 4 mM increased the secretion of S100A7 and lactoferrin as well as the intracellular concentration of β-defensin 1 and cathelicidin 7 in cultured MECs. In addition, an intravenous injection of Valine increased S100A7 levels in the milk of Tokara goats without influencing milk yield and milk components (i.e., fat, protein, lactose, and solids). In contrast, Valine treatment did not affect TJ barrier function either in vitro or in vivo. These findings indicate that Valine enhances antimicrobial component production without influencing milk production and TJ barrier function in lactating mammary glands; thus, Valine contributes to safe dairy production.

Relationship of the pool of intracellular Valine to protein synthesis and degradation in cultured cells

J Biol Chem 1976 Jul 25;251(14):4458-7.PMID:932042doi

To explore the role of the pool of intracellular free Valine in the processes of protein synthesis and protein degradation, cultured hepatoma (HTC) cells were incubated in media containing varying concentrations of L-valine, under conditions of constant rates of protein synthesis and protein breakdown, and at steady state levels of intracellular Valine specific radioactivities. Two types of experiments were compared: in the first (designated "incorporation experiment"), unlabeled cells were exposed to [3H]Valine for a short period of time. In the second (termed "reincorporation experiment"), cells were prelabled with [3H]Valine and then incubated for a brief period with media containing different concentrations of unlabeled Valine; reincorporation of [3H]Valine was calculated by the difference between the release of [3H]Valine from labeled cellular proteins at low Valine concentrations, and the maximal rate of the release at high Valine concentrations. In both types of experiments, the rates of [3H]Valine incorporation or reincorporation were compared with the respective specific radioactivities of free intracellular Valine. In the incorporation experiment, the rates of [3H]Valine incorporation into protein calculated by the intracellular specific radioactivities were not constant, but showed an upward deviation at low Valine concentrations. This is in agreement with the results of Mortimore, G.E., Woodside, K.H., and Henry, J.E. ((1972) J. Biol. Chem. 247, 2776-2784) in the perfused rat liver. By contrast, in the reincorporation experiment, the calculated rates of [3H]Valine reincorporation based on intracellular specific radioactivities were constant throughout the range of Valine concentrations. The constant value of calculated Valine reincorporation was lower by 30 to 50% than the calculated rate of Valine incorporation at high Valine concentrations. The following model is proposed to explain these results. There is one common pool of free intracellular Valine, but there are two sites where valyl-tRNA can be formed. The first is an internal site that utilizes Valine from the intracellular pool, and the second is an external (possibly membranous) system that converts extracellular Valine directly to valyl-tRNA. Valine originating from protein degradation flows into the intracellular pool, from which it can be reutilized by the internal system. According to these assumptions, in the incorporation experiment and at low Valine concentrations, the specific activity of valyl-tRNA is higher than that of the intracellular pool of free Valine, due to the contribution of the external system. On the other hand, in the reincorporation experiment the specific activity of extracellular Valine is negligible in comparison with that of the intracellular pool. Therefore, in this case the specific activity of valyl-tRNA is proportional to that of the intracellular pool, with a constant dilution by unlabeled Valine of extracellular origin...

Valine kinetics at graded Valine intakes in young men

Am J Clin Nutr 1986 May;43(5):781-6.PMID:3706188DOI:10.1093/ajcn/43.5.781.

Twelve young men, six subjects in each group studied in two phases, participated in an experiment to explore the relationships between Valine intake, plasma Valine concentrations, and Valine kinetics, using 1-[13C]Valine as a tracer. Below a Valine intake of about 20 mg.kg-1.day-1 plasma Valine concentrations reached a low and relatively constant level. The rate of Valine oxidation fell with the decline in the intake of amino acid. Below Valine intakes of 16 mg.kg-1.day-1, the mean daily rate of oxidation was estimated to be generally higher than the intake level, implying a negative Valine balance during the 24 h day. These findings indicate that an intake of 10 mg Valine kg-1.day-1 would not be adequate to maintain protein nutritional status. Our results are discussed in relation to the currently accepted 1973 FAO/WHO value of 10 mg.kg-1.day-1 as being the upper range of the Valine requirement in healthy adult humans.